ID   NPIID_ARTGP             Reviewed;         371 AA.
AC   E4US45;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Neutral protease 2 homolog MGYG_03465;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin MGYG_03465;
DE   Flags: Precursor;
GN   ORFNames=MGYG_03465;
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- FUNCTION: Secreted metalloproteinase that allows assimilation of
CC       proteinaceous substrates. Shows high activities on basic nuclear
CC       substrates such as histone and protamine. May be involved in virulence
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage of bonds with hydrophobic residues in
CC         P1'. Also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain.;
CC         EC=3.4.24.39;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M35 family. {ECO:0000305}.
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DR   EMBL; DS989824; EFR00463.1; -; Genomic_DNA.
DR   RefSeq; XP_003173293.1; XM_003173245.1.
DR   AlphaFoldDB; E4US45; -.
DR   SMR; E4US45; -.
DR   MEROPS; M35.001; -.
DR   EnsemblFungi; EFR00463; EFR00463; MGYG_03465.
DR   GeneID; 10028555; -.
DR   eggNOG; ENOG502SGF5; Eukaryota.
DR   HOGENOM; CLU_039313_1_0_1; -.
DR   InParanoid; E4US45; -.
DR   OMA; ESNELHM; -.
DR   OrthoDB; 1038868at2759; -.
DR   Proteomes; UP000002669; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001384; Peptidase_M35.
DR   Pfam; PF02102; Peptidase_M35; 1.
DR   PRINTS; PR00768; DEUTEROLYSIN.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Disulfide bond; Hydrolase;
KW   Metal-binding; Metalloprotease; Protease; Reference proteome; Secreted;
KW   Signal; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..188
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407140"
FT   CHAIN           189..371
FT                   /note="Neutral protease 2 homolog MGYG_03465"
FT                   /id="PRO_0000407141"
FT   ACT_SITE        317
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         316
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         320
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         331
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   DISULFID        196..267
FT                   /evidence="ECO:0000250"
FT   DISULFID        274..292
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   371 AA;  40240 MW;  FDEC1906F71C4F4A CRC64;
     MQFVAVLAAL GALVAPAAAY PHAPMNETLV DVQLTAVGNT MVKATITNKG DSVLNMLQFN
     TIMDENPTRK VMVFQDGVEV PFTGMMPRYL MSDLTEEFFT TLPPQASVEH TFDIAATHDL
     SAGGKYVISA SGAVPTAEEH STTITSTALY ESNELHMEVD GVQAAAVEQA MNFTPEMQSI
     HARALEKRTK IVSGSCNQNT LRATMNALGN SARLAQAASR AASQNPRKFQ EYFRTNDANA
     KQRVIARLNS VARESSSANA GVTTYYCSDT MGGCKPRVLA YTLPSRNLVV NCPIYYNLPP
     LTKQCHAQDQ ATTTLHEFTH NPAVASPHCQ DYAYGYQQCI SLPAAKAVQN ADNYALFANG
     MLSNLFVFTL N